| Product Name | Fish Lipid Peroxide (LPO) ELISA Kit |
|---|---|
| Description | Fish Lipid Peroxide (LPO) ELISA Kit has high sensitivity and excellent specificity for detection of FishLPO. No significant cross-reactivity or interference between FishLPO and analogues was observed. Lactoperoxidase is a peroxidase enzyme found in milk. It is able to form reactive bromine and iodine species, resulting in natural organobromine and organoiodine substances, and can therefore be categorised as a haloperoxidase. It is fairly heat resistant and was widely used as an indicator of overpasteurization of milk.Freshly isolated and purified samples of goat LPO were saturated with ammonium iodide and crystallized using 20% polyethylene glycol 3350 in a hanging drop vapor diffusion setup. Goat LPO consists of a single polypeptide chain of 595 amino acid residues and folds into an oval-shaped structure. The structure contains 20 well-defined alpha-helices of varying lengths including a helix, H(2a), unique to LPO, and two short antiparallel beta-strands. This Fish Lipid Peroxide (LPO) ELISA Kit employs a two-site sandwich ELISA to quantitate LPO in samples. An antibody specific for LPO has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyLPO present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for LPO is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of LPO bound in the initial step. The color development is stopped and the intensity of the color is measured. |
| Synonyms | LPO, MGC129990, MGC129991, SPO, salivary peroxidase |
| Method | Sandwich ELISA |
| Detection Range | Please inquire |
| Sensitivity | Please inquire |
| Reactivity | Fish |
| Sample Types | Cell culture supernatants, Serum, Plasma, Other biological fluids |
| Storage | 2-8°C |
| Background | Lactoperoxidase is a peroxidase enzyme found in milk. It is able to form reactive bromine and iodine species, resulting in natural organobromine and organoiodine substances, and can therefore be categorised as a haloperoxidase. It is fairly heat resistant and was widely used as an indicator of overpasteurization of milk.Freshly isolated and purified samples of goat LPO were saturated with ammonium iodide and crystallized using 20% polyethylene glycol 3350 in a hanging drop vapor diffusion setup. Goat LPO consists of a single polypeptide chain of 595 amino acid residues and folds into an oval-shaped structure. The structure contains 20 well-defined alpha-helices of varying lengths including a helix, H(2a), unique to LPO, and two short antiparallel beta-strands. |
| Supplier | Abbkine |
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